› 3c5l

X-ray diffraction
2.33Å resolution

Polo-like kinase 1 Polo box domain in complex with PPHSpT peptide

Released:
DOI: 10.2210/pdb3c5l/pdb
PDB entry 3c5l coloured by chain, front view.
PDB entry 3c5l coloured by chain, side view.
PDB entry 3c5l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1.
Yun SM, Moulaei T, Lim D, Bang JK, Park JE, Shenoy SR, Liu F, Kang YH, Liao C, Soung NK, Lee S, Yoon DY, Lim Y, Lee DH, Otaka A, Appella E, McMahon JB, Nicklaus MC, Burke TR, Yaffe MB, Wlodawer A, Lee KS
Nat Struct Mol Biol 16 876-82 (2009)
PMID: 19597481

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156756 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase PLK1 Chain: A
Molecule details ›
Chain: A
Length: 221 amino acids
Theoretical weight: 25.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53350 (Residues: 373-593; Coverage: 37%)
Gene names: PLK, PLK1
Sequence domains: POLO box duplicated region
Structure domains: POLO box domain
Peptide Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 619 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 35.442Å b: 66.495Å c: 105.817Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.246 0.246 0.293
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

17 review citations

Polo-box domain: a versatile mediator of polo-like kinase function.
Park et al. (2010)
16 more

7 mentions without citation

Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1.
Yun et al. (2009)
6 more